NMAT1_ARATH
ID NMAT1_ARATH Reviewed; 711 AA.
AC Q9C8R8;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Nuclear intron maturase 1, mitochondrial {ECO:0000303|PubMed:19946041};
DE Short=AtnMat1 {ECO:0000303|PubMed:19946041};
DE EC=3.1.-.-;
DE AltName: Full=Nuclear intron maturase 1 a {ECO:0000303|PubMed:12527773};
DE Short=AtnMat1a {ECO:0000303|PubMed:12527773};
DE AltName: Full=Protein CHANGED SENSITIVITY TO CELLULOSE SYNTHESIS INHIBITORS 1 {ECO:0000303|PubMed:16621844};
DE Flags: Precursor;
GN Name=NMAT1 {ECO:0000303|PubMed:19946041};
GN Synonyms=CSS1 {ECO:0000303|PubMed:16621844},
GN NMAT1A {ECO:0000303|PubMed:12527773};
GN OrderedLocusNames=At1g30010 {ECO:0000312|Araport:AT1G30010};
GN ORFNames=T1P2.4 {ECO:0000312|EMBL:AAG52062.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY.
RX PubMed=12527773; DOI=10.1093/nar/gkg153;
RA Mohr G., Lambowitz A.M.;
RT "Putative proteins related to group II intron reverse
RT transcriptase/maturases are encoded by nuclear genes in higher plants.";
RL Nucleic Acids Res. 31:647-652(2003).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16621844; DOI=10.1093/pcp/pcj051;
RA Nakagawa N., Sakurai N.;
RT "A mutation in At-nMat1a, which encodes a nuclear gene having high
RT similarity to group II intron maturase, causes impaired splicing of
RT mitochondrial NAD4 transcript and altered carbon metabolism in Arabidopsis
RT thaliana.";
RL Plant Cell Physiol. 47:772-783(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP SUBCELLULAR LOCATION, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=19946041; DOI=10.1261/rna.1776409;
RA Keren I., Bezawork-Geleta A., Kolton M., Maayan I., Belausov E., Levy M.,
RA Mett A., Gidoni D., Shaya F., Ostersetzer-Biran O.;
RT "AtnMat2, a nuclear-encoded maturase required for splicing of group-II
RT introns in Arabidopsis mitochondria.";
RL RNA 15:2299-2311(2009).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=22429648; DOI=10.1111/j.1365-313x.2012.04998.x;
RA Keren I., Tal L., des Francs-Small C.C., Araujo W.L., Shevtsov S.,
RA Shaya F., Fernie A.R., Small I., Ostersetzer-Biran O.;
RT "nMAT1, a nuclear-encoded maturase involved in the trans-splicing of nad1
RT intron 1, is essential for mitochondrial complex I assembly and function.";
RL Plant J. 71:413-426(2012).
RN [8]
RP REVIEW ON SPLICING FACTORS.
RC STRAIN=cv. Columbia;
RX PubMed=24600456; DOI=10.3389/fpls.2014.00035;
RA Brown G.G., Colas des Francs-Small C., Ostersetzer-Biran O.;
RT "Group II intron splicing factors in plant mitochondria.";
RL Front. Plant Sci. 5:35-35(2014).
CC -!- FUNCTION: Nuclear-encoded maturase required for splicing of group-II
CC introns in mitochondria (PubMed:16621844, PubMed:22429648). Necessary
CC for mitochondrial biogenesis during early developmental stages
CC (PubMed:22429648). Involved in the splicing of mitochondrial NAD4
CC transcripts (PubMed:16621844). Required for trans-splicing of NAD1
CC intron 1 and also functions in cis-splicing of NAD2 intron 1 and NAD4
CC intron 2 (PubMed:22429648). Required for the regulation of fundamental
CC metabolic pathways such as amino acid metabolism, triacylglycerol
CC degradation and polysaccharide synthesis (cellulose and starch) during
CC the early stage of plant growth (PubMed:16621844). Implicated in stress
CC responses (PubMed:22429648). {ECO:0000269|PubMed:16621844,
CC ECO:0000269|PubMed:22429648}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19946041}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in seedlings and
CC accumulates in adult plants. {ECO:0000269|PubMed:16621844}.
CC -!- DISRUPTION PHENOTYPE: Slightly slower growth rate. Impaired splicing of
CC mitochondrial group-II introns-containing NAD4 transcript and altered
CC carbon metabolism. Altered fundamental metabolic pathways including
CC amino acid metabolism, triacylglycerol degradation and polysaccharide
CC synthesis (cellulose and starch) during the early stage of plant
CC growth. Reduced sensitivity to 2,6-dichlorobenzonitrile (DCB) and
CC isoxaben treatments, cellulose biosynthesis inhibitors. Increased
CC sensitivity to sugar concentration of the medium (PubMed:16621844).
CC Retarded growth and developmental phenotypes (e.g. reduced germination
CC efficiency, altered primary root elongation and impaired vegetative
CC growth and fertility) and modified respiration activities. Altered
CC stress responses characterized by high levels accumulation of reactive
CC oxygen species (ROS) and darker and reddish leaves. Abnormal
CC mitochondrial morphology (PubMed:22429648).
CC {ECO:0000269|PubMed:16621844, ECO:0000269|PubMed:22429648}.
CC -!- SIMILARITY: Belongs to the plant nuclear intron maturase (nMat) family.
CC {ECO:0000305}.
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DR EMBL; AC022455; AAG52062.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31167.1; -; Genomic_DNA.
DR PIR; A86424; A86424.
DR RefSeq; NP_174294.1; NM_102741.3.
DR AlphaFoldDB; Q9C8R8; -.
DR STRING; 3702.AT1G30010.1; -.
DR PaxDb; Q9C8R8; -.
DR PRIDE; Q9C8R8; -.
DR ProteomicsDB; 251117; -.
DR EnsemblPlants; AT1G30010.1; AT1G30010.1; AT1G30010.
DR GeneID; 839880; -.
DR Gramene; AT1G30010.1; AT1G30010.1; AT1G30010.
DR KEGG; ath:AT1G30010; -.
DR Araport; AT1G30010; -.
DR TAIR; locus:2198309; AT1G30010.
DR eggNOG; KOG1075; Eukaryota.
DR HOGENOM; CLU_009993_1_0_1; -.
DR InParanoid; Q9C8R8; -.
DR OMA; LIPSCDY; -.
DR OrthoDB; 356246at2759; -.
DR PhylomeDB; Q9C8R8; -.
DR PRO; PR:Q9C8R8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8R8; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0000373; P:Group II intron splicing; IMP:UniProtKB.
DR GO; GO:0000374; P:Group III intron splicing; IMP:TAIR.
DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR GO; GO:0090615; P:mitochondrial mRNA processing; IMP:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; IMP:UniProtKB.
DR GO; GO:2001006; P:regulation of cellulose biosynthetic process; IMP:UniProtKB.
DR GO; GO:0032885; P:regulation of polysaccharide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010896; P:regulation of triglyceride catabolic process; IMP:UniProtKB.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR GO; GO:0090351; P:seedling development; IMP:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR024937; Domain_X.
DR Pfam; PF01348; Intron_maturas2; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
PE 1: Evidence at protein level;
KW Endonuclease; Hydrolase; Intron homing; Mitochondrion; Nuclease;
KW Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..711
FT /note="Nuclear intron maturase 1, mitochondrial"
FT /id="PRO_0000440119"
FT DOMAIN 147..459
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT REGION 484..653
FT /note="Intron maturase type-2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 711 AA; 81537 MW; C27CBC2A1D809982 CRC64;
MKRLTYPLSS LRNIVEHFHC NTFHKPISSL SISPTLKSES REPSSTQDPY SLLKQDPVDI
CLSLWVKSFS SPPSATFSNL TGFLSKFDLW VLAYQRTCAH VTGTFPPRNA IHANALRSLL
SLQNAVTRSG GKFRWNDKMN QYVRSPKDKI SMNGGEGMSK GKVRRIIESE EPIFQDRVVH
EVLLMILEPF FEARFSSKSH GFRPGRNPHT VIRTIRSNFA GYLWFMKGDV SEMLDHVDVD
VVMNCLQKVV KDRKVLGLIE SSLKFSDKRV LKRVVEKHGN DNGLGTKRRI EREKRNKTKK
KILSDDEPKP DPYWLRTFYS FAPKEAAKVP SYGYCGVLSP LLANVCLNEL DRFMETKIVE
YFSPCKDDSI WKESIEDGCH NPAWPEFVPS SGKEKTRKMD YIRYGGHFLI GIRGPREDAV
KMRKEIIDFC DRVFGVRLDN SKLEIEHISR GIQFLDHIIC RRVIYPTLRY TGSGGSIVSK
KGVGTLLSVS ASLEQCIRQF RRLAFVKGDK DPEPLPCNPM LYSSQSHSNS QMNKFLETMA
DWYKYADNRK KAVGFCAYVI RSSLAKLYAA RYRLKSRAKV YSIASRDLSH PLSESSNNSA
PEYSDLLRMG LVDAIEGVQF SRMSLIPSCD YTPFPRNWIP NHEQVLQEYI RLQDPKFFCG
LHRSIKREGL TLPQDEISEA VWDFKTLGAW RSKYENKREA DDGLQKLDSQ T
